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|Title:||Thermal unfolding of hen egg-white lysozyme in the presence of 4-chlorobutan-1-ol|
|Keywords:||Differential Scanning Calorimetry|
Partially Folded State
|Publisher:||BLACKWELL SCIENCE LTD|
|Citation:||PURE AND APPLIED CHEMISTRY,70(3)665-670|
|Abstract:||High sensitivity differential scanning calorimetry transitions for the highly irreversible thermal denaturation of hen egg white lysozyme in the presence of low concentration (<250 mM) of 4-chlorobutan-1-ol are strongly scanning rate dependent, suggesting that the denaturation is at least in part, under kinetic control The scan rate dependence can be examined by assuming that the thermal denaturation takes place to the kinetic scheme [GRAPHICS] where k(3) >> k(2), thus the data fitting to the extreme case of this model ie. N --> F where N is the native state, D is the unfolded one and F is the final irreversibly arrived state. However, the thermal denaturation in the presence of 3-chloro-propan- 1-ol, 3-chloropropan-1,2-diol and their corresponding normal alcohols was earlier(ref 1) observed to be reversible two-state.|
|Appears in Collections:||Proceedings papers|
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